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KCHIP1蛋白的两个新功能域研究

刘征, 肖向军, 樊飞跃, 孙元明, 李雨民, 杨福军

中国医学科学院,中国协和医科大学,放射医学研究所. 天津 300192；Roy J.and Lucille A.Carver College of Medicine,The University of Iowa. 美国

摘要

Homo sapiens Kvchannel interacting protein 1(KCHIP1)基因表达蛋白是新发现的神经钙离子结合蛋白超家族中的一个新成员.该文利用定点突变和荧光定位等技术,证实KCHIP1蛋白具有钙离子结合域和肉豆蔻酰化位点两个显著的结构特点,同时发现了KCHIP1蛋白两个对肉豆蔻酰化有重要意义的肉豆蔻酰化位点G2A和G6A。

关键词： 钙离子; 肉豆蔻酰化; 定点突变

Experimental study on the new significant function domains of KCHIP1 protein

Liu Xheng, Xiao Xiangjunn, Fan Feiyue, Sun Yuanming, Li Yumin, Yang Fujun

Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College. Tianjin 300192, China；Roy J. and Lucille A. Carver College of Medicine, The University of Iowa. USA

Abstract

Human Kv channel interacting protein 1 (KCHIP1) is a new member of the neural calcium binding protein superfamily. Theoretically KCHIP1 has several calcium binding domains and two myristoylation sites. In this study, we demonstrated that the calcium binding domains and myristoylation sites were functional. The first, through running SDS-PAGE gel, we testified its ability of binding Ca~(2+) with obvious discrepancy of the electrophoresis migrating rate after binding Ca~(2+). Then, through the techniques of fused green fluorescence protein and site-directed mutagenesis, we demonstrated that wild type KCHIP1 protein accumulated in the secretory vesicles of Golgi body. In contrast, its two mutated forms without myristoylation sites accumulated throughout the whole cytoplasm. These observations indicate that KCHIP1 protein has a myristoylation motif mediating the interaction between KCHIP1 protein and membrane.

Key words: Ca~(2+);Myristoylation;Site-directed mutagenesis

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引用本文：

刘征, 肖向军, 樊飞跃, 孙元明, 李雨民, 杨福军. KCHIP1蛋白的两个新功能域研究[J]. 生理学报 2005; 57 (3): .

Liu Xheng, Xiao Xiangjunn, Fan Feiyue, Sun Yuanming, Li Yumin, Yang Fujun. Experimental study on the new significant function domains of KCHIP1 protein. Acta Physiol Sin 2005; 57 (3): (in Chinese with English abstract).